Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites

Poly(ADP-ribose) polymerase 1 (PARP1) synthesizes poly(ADP-ribose) (PAR) using nicotinamide adenine dinucleotide (NAD) as a substrate. Despite intensive research on the cellular functions of PARP1, the molecular mechanism of PAR formation has not been comprehensively understood. In this study, we el...

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Bibliographic Details
Published in:	Nucleic acids research Vol. 37; no. 11; pp. 3723 - 3738
Main Authors:	Altmeyer, Matthias, Messner, Simon, Hassa, Paul O, Fey, Monika, Hottiger, Michael O
Format:	Journal Article
Language:	English
Published:	England Oxford University Press 01.06.2009 Oxford Publishing Limited (England)
Subjects:	active sites Adenosine diphosphate Catalytic Domain Cell Cycle Proteins - chemistry Cell Cycle Proteins - metabolism Deoxyribonucleic acid DNA DNA - metabolism DNA-binding domains glutamic acid Glutamic Acid - metabolism Humans lysine Lysine - metabolism NAD (coenzyme) NAD ADP-ribosyltransferase nucleic acids Nucleic Acids Enzymes Poly (ADP-Ribose) Polymerase-1 Poly Adenosine Diphosphate Ribose - metabolism Poly(ADP-ribose) Polymerases - chemistry Poly(ADP-ribose) Polymerases - metabolism Protein Multimerization Protein Structure, Tertiary recombinant fusion proteins
ISSN:	0305-1048, 1362-4962, 1362-4962
Online Access:	Get full text
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